3ZHW
X-ray Crystallographic Structural Characteristics of Arabidopsis Hemoglobin I and their Functional Implications
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0001666 | biological_process | response to hypoxia |
| A | 0005344 | molecular_function | oxygen carrier activity |
| A | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0009505 | cellular_component | plant-type cell wall |
| A | 0009506 | cellular_component | plasmodesma |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0071456 | biological_process | cellular response to hypoxia |
| B | 0001666 | biological_process | response to hypoxia |
| B | 0005344 | molecular_function | oxygen carrier activity |
| B | 0005634 | cellular_component | nucleus |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0009505 | cellular_component | plant-type cell wall |
| B | 0009506 | cellular_component | plasmodesma |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0020037 | molecular_function | heme binding |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0071456 | biological_process | cellular response to hypoxia |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM A 1163 |
| Chain | Residue |
| A | LYS65 |
| A | PHE114 |
| A | ALA117 |
| A | LEU148 |
| A | HOH2022 |
| A | HOH2045 |
| A | HOH2071 |
| B | LEU158 |
| B | ASN160 |
| A | HIS69 |
| A | SER72 |
| A | ARG99 |
| A | LEU100 |
| A | SER103 |
| A | HIS104 |
| A | TYR107 |
| A | HIS113 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1902 |
| Chain | Residue |
| A | LYS126 |
| A | TRP133 |
| A | LYS138 |
| A | HOH2049 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1904 |
| Chain | Residue |
| A | LYS118 |
| A | VAL139 |
| A | GLY142 |
| A | GLN143 |
| A | ASP146 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 1905 |
| Chain | Residue |
| A | LEU53 |
| A | ARG54 |
| A | LYS65 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM B 1163 |
| Chain | Residue |
| B | PHE50 |
| B | LYS65 |
| B | HIS69 |
| B | ARG99 |
| B | LEU100 |
| B | SER103 |
| B | HIS104 |
| B | TYR107 |
| B | HIS113 |
| B | PHE114 |
| B | ALA117 |
| B | VAL149 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 B 1906 |
| Chain | Residue |
| B | LYS126 |
| B | TRP133 |
| B | LYS138 |
| B | HOH2046 |
| B | HOH2056 |
Functional Information from PROSITE/UniProt
| site_id | PS00208 |
| Number of Residues | 12 |
| Details | PLANT_GLOBIN Plant hemoglobins signature. NPkLkpHAmsvF |
| Chain | Residue | Details |
| A | ASN63-PHE74 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 298 |
| Details | Domain: {"description":"Globin","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Motif: {"description":"Homodimerization","evidences":[{"source":"PubMed","id":"23485912","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ZHW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"P68168","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"23485912","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ZHW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"distal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23485912","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ZHW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"O04986","evidenceCode":"ECO:0000250"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Binding site: {"description":"proximal binding residue","evidences":[{"source":"PROSITE-ProRule","id":"PRU00238","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"23485912","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ZHW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Site: {"description":"Homodimerization","evidences":[{"source":"PubMed","id":"23485912","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3ZHW","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
